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One of the most prominent characteristics of metallothionein (MT) is its high cysteine content of 30%. The sulfhydryl groups, normally involved in metal binding, render the protein particularly sensitive towards oxidation. Oxidation of sulfhydryl groups in MT may occur in vivo and in vitro, either intra- or intermolecularly, the latter leading to dimeric or polymeric forms of MT. Thiol oxidation and oligomerization of MT may be induced by various radicals (
1-3
) and free metal ions (
4
). The sensitivity to oxidation of thiol groups in MT to a great extent depends on the metals that are bound to the protein. Particularly the Cu-containing MT easily polymerizes (
3,5
). Accordingly, Cu-rich polymerized MT has been isolated from the livers of newborn animals (
6
) and human fetuses (
7,8
). Insoluble polymerized forms of MT were shown to be mainly located in the heavy lysosomal fraction of the liver (
6
). In agreement, elevated levels of Cu associated with oxidized forms of MT have been described in lysosomes of patients with Wilson disease and dogs with inherited Cu-toxicosis (
9-12
). More recently, polymeric MT has been also detected in lysosomes of hepatocytes and Kupffer cells from LEC rats, the rodent model for Wilson disease (
13
).